SRC2_XENLA
ID SRC2_XENLA Reviewed; 532 AA.
AC P13116;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Tyrosine-protein kinase Src-2;
DE EC=2.7.10.2;
DE AltName: Full=p60-Src-2;
GN Name=src-b; Synonyms=src2;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2499582; DOI=10.1016/s0021-9258(18)81671-4;
RA Steele R.E., Unger T.F., Mardis M.J., Fero J.B.;
RT "The two Xenopus laevis SRC genes are co-expressed and each produces
RT functional pp60src.";
RL J. Biol. Chem. 264:10649-10653(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 439-492.
RC TISSUE=Erythrocyte;
RX PubMed=2987836; DOI=10.1093/nar/13.5.1747;
RA Steele R.E.;
RT "Two divergent cellular src genes are expressed in Xenopus laevis.";
RL Nucleic Acids Res. 13:1747-1761(1985).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC kinase family. SRC subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M23422; AAA49961.1; -; mRNA.
DR EMBL; AH002584; AAA51644.1; -; Genomic_DNA.
DR PIR; B34104; B34104.
DR RefSeq; XP_018096693.1; XM_018241204.1.
DR AlphaFoldDB; P13116; -.
DR SMR; P13116; -.
DR DNASU; 380430; -.
DR GeneID; 380430; -.
DR CTD; 380430; -.
DR Xenbase; XB-GENE-489824; src.L.
DR OrthoDB; 539311at2759; -.
DR BRENDA; 2.7.10.2; 6725.
DR Proteomes; UP000186698; Chromosome 9_10L.
DR Bgee; 380430; Expressed in blastula and 19 other tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR Pfam; PF00017; SH2; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR PRINTS; PR00452; SH3DOMAIN.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00252; SH2; 1.
DR SMART; SM00326; SH3; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Cell membrane; Kinase; Lipoprotein; Membrane; Myristate;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; SH2 domain;
KW SH3 domain; Transferase; Tyrosine-protein kinase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..532
FT /note="Tyrosine-protein kinase Src-2"
FT /id="PRO_0000088146"
FT DOMAIN 80..141
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 147..244
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 266..519
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 385
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028"
FT BINDING 272..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 294
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 415
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000250"
FT LIPID 2
FT /note="N-myristoyl glycine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 532 AA; 59737 MW; ED04A4D1492ECE2B CRC64;
MGATKSKPRE GGPRSRSLDI AEGSHQPFTS LSASQTPSKS LDSHRPSGQP FGGNCDLTPF
GGVNFSDTIT SPQRTGPLAG GVTTFVALYD YESRTETDLS FRKGERLQIV NNTEGDWWLA
RSLSSGQTGY IPSNYVAPSD SIQAEEWYLG KITRREAERL LLSLENPRGT FLVRESETTK
GAYCLSVSDY DASRGLNVKH YKIRKLDSGG FYITSRTQFS SLQQLVAYYS KHADGLCHRL
TAVCPTAKPQ TQGLSKDAWE IPRDSLRLEL KLGQGCFGEV WMGTWNGTTR VAIKTLKPGT
MSPEAFLQEA QVMKKLRHEK LVQLYAVVSE EPIYIVTEYM SKGSLLDFLK GEMGRYLRLP
QLVDMAAQIA SGMAYVERMN YVHRDLRAAN ILVGENLVCK VADFGLARLI EDNEYTARQG
AKFPIKWTAP EAALYGRFTI KSDVWSFGIL LTELTTKGRV PYPGMVNREV LDQVERGYRM
PCPPDCPESL HDLMFQCWRK DPEERPTFEY LQAFLEDYFT ATEPQYQPGD NL
